ID   P74451_SYNY3            Unreviewed;       631 AA.
AC   P74451;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAA18552.1};
GN   OrderedLocusNames=slr0152 {ECO:0000313|EMBL:BAA18552.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA18552.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA18552.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; BA000022; BAA18552.1; -; Genomic_DNA.
DR   PIR; S76423; S76423.
DR   AlphaFoldDB; P74451; -.
DR   SMR; P74451; -.
DR   IntAct; P74451; 6.
DR   STRING; 1148.gene:10499434; -.
DR   PaxDb; 1148-1653640; -.
DR   EnsemblBacteria; BAA18552; BAA18552; BAA18552.
DR   KEGG; syn:slr0152; -.
DR   eggNOG; COG0515; Bacteria.
DR   InParanoid; P74451; -.
DR   PhylomeDB; P74451; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF116; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAA18552.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001425};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAA18552.1};
KW   Transferase {ECO:0000313|EMBL:BAA18552.1}.
FT   DOMAIN          29..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   631 AA;  70660 MW;  AD14A789C8FB3E34 CRC64;
     MESLPVLGVF FMVKTANVAV MPLFPRSQYR IIGQIGQGQF GRVYCAIHRT TGKMYALKDL
     EHRVFPTNKF LRELSYLLTL RHPNIVACHG LEYHPGGRYL VMDYCEGGTL RDIIDGDGDL
     CLAGKIDLLR QILLGLAQAH QHDIVHCDLK PENILLIPRA EGWQVKVSDF GIARLTAKTG
     NPNFSKGYTG SPAYMAPERF YGKFSVASDI YAVGILLYEL IVGDRPFSGF PKALQAAHLN
     VRLTLPPEFP PLLAPIVQRA LEKLPQRRFP NATAMASDLA TVQKQILEQD PPRGNGYLYH
     HLAPAPLAFT ATVKHSTPLL FPISHLTGAG LWLYLGNGAE LYLWEYGDGN VEHHPLPRWA
     LGLPGTIANL EVNQDQISLL IQGGEPGEWQ FYQWRETLLG ALSLPKPRIN LRAERLLANL
     SPGGKTLAVV VGDRDSEKGH FQLWRTDHSL PVAAAVVIRW PDQLLTLDQN HGLLVQSQST
     ASYCHTIFFL FNRRGSLFPA FRLSFLVFQL VVNRYSRNHL FGLADNAPYT GILIRLQPLK
     VNRIALTIQP QFIEPFPWGY LLADRHGEVA LLDYEGFLFG NFSLGETITA IAPMGRYLCL
     FATWQGNGGT LRLLDLGPQV ENIIRQRQEK R
//